Protein architecture: assembly of ordered films by means of alternated adsorption of oppositely charged macromolecules.
Methods of making molecularly ordered protein films are reviewed with special reference to the recently developed technique of protein multilayer assembly by alternated adsorption of opposite-charge polyions. This method has been applied for linear and branched polyions, DNA, polynucleotides, proteins, viruses and clay nanoplates. This provides good prospects for biomolecular architecture. Quartz crystal microbalance, X-ray and neutron reflectivity, scanning electron microscopy, atomic force microscopy and UV-absorbance data are used to analyze the film structure. Multilayer buildup by alternation of polyions and 16 different charged proteins is discussed. In most cases, enzymes in the films retained their activity. Protein/ceramic nanoplates consisting of alternated montmorillonite clay and glucose oxidase layers electrostatically linked by polycations were also assembled. Protein layers can be arranged according to specific biological activity. Consecutive enzymic reactions were performed in anisotropic protein layers prepared with precise control of distances between the active layers (1-50 nm). Film superlattices containing ordered layers of more than one protein were constructed using myoglobin, lysozyme, peroxidase, glucoamylase, glucose oxidase and catalase. Glucoamylase, glucose oxidase/peroxidase catalyze the starch-glucose-H2020 reaction. The reaction products and nonreacting starch were separated by filtration when the substrate solution passed through the multienzyme films assembled on a filter. Formation of alternate outermost layers (of opposite charge or opposite specificity) at every adsorption cycle is the key point of the layer-by-layer assembly. Multilayers were obtained by alternated adsorption of concanavalin A and glycogen (or streptavidin and biotinylated polylysine) were designed using their biospecific interaction. Protein films are of extreme interest as novel biologically active materials.
Lvov YuM
Institute of Crystallography, Russian Academy of Sciences, Moscow.
Sukhorukov
G B
GB
D000327:Adsorption; D001709:Biotechnology / Q000379:methods*; D007477:Ions; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties
D007477:Ions; D011506:Proteins